A possible role of Cu2+ ions in bovine antibody-antigen interactions.
A preparation of purified bovine IgG1 was found to contain 0.5 moles of Cu2+ ions per mole of protein. Scatchard analysis of the binding of Cu2+ ions to bovine IgG1 indicated the presence of 4 +/- 1 binding sites with an affinity of 2 x 10(5) M-1. Calculations indicate that in bovine plasma, IgG1 will not compete significantly with albumin for Cu2, whereas a proportion of Cu2+ may well be bound to IgG1 in colostrum. Physiological levels of Cu2+ were found to enhance the interaction between IgG1 antibody and Brucella abortus in the presence of albumin. Irrespective of whether IgG1 binds Cu2+ in vivo, it is possible that Cu2+ can influence the results of serological tests.
D000818:Animals; D000937:Antigen-Antibody Reactions / Q000187:drug effects*; D000942:Antigens, Bacterial / Q000276:immunology; D001666:Binding Sites, Antibody / Q000187:drug effects; D002003:Brucella abortus / Q000276:immunology; D002417:Cattle / Q000276:immunology*; D003300:Copper / Q000032:analysis / Q000494:pharmacology*; D007074:Immunoglobulin G / Q000032:analysis
D000942:Antigens, Bacterial; D007074:Immunoglobulin G; D003300:Copper